THE PROTEOME HOMOLOGY OF PEPTIDES EXTRACTED FROM DRY-CURED XUANWEI HAM Lujuan Xing, Xiaoge Gao, Guanghong Zhou and Wangang Zhang* Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control; Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China. *Corresponding author email:
[email protected] Abstract –The objective of this study was to investigate the proteome homology of peptides purified from dry- cured Xuanwei ham. The Xuanwei ham peptides (XHP) were extracted and then LC-ESI-Q-TOF-MS/MS connected with Proteome Discoverer was used to analyze the peptide compositions. The results showed that there were 93 peptides identified in Xuanwei ham. The proteome homology results showed that myosin was the main protein for the generation of peptides accounting for 39% of all peptides. Hydrophobic amino acids accounted for 21% of free amino acids, among which Glu and His were the main amino acids. The abundant composition of peptides and free amino acid may endow the special flavor and characteristic for Xuanwei ham. Key Words – Peptides; Proteome homology; Amino acid composition. I. INTRODUCTION Xuanwei ham is produced in Xuanwei city of Yunnan province and the special climatic condition contributes to the unique flavor and texture for dry-cured hams. During the long ripening time, intense proteolysis is formed in ham muscles and 10% of muscle proteins including soluble and insoluble proteins could be degraded[1]. Intense protein degradation results in the accumulation of peptides with different sizes and free amino acids at the end of processing. Many studies have reported that bioactive peptides could be produced in dry-cured hams, while no studies have studied the proteome homology of these bioactive peptides in Xuanwei ham.